[1]	NUCLEOTIDE SEQUENCE [MRNA]. PubMed=1674604 [NCBI, ExPASy, EBI, Israel, Japan] Gubler U., Chua A.O., Schoenhaut D.S., Dwyer C.M., McComas W., Motyka R., Nabavi N., Wolitzky A.G., Quinn P.M., Familletti P.C., Gately M.K.; "Coexpression of two distinct genes is required to generate secreted bioactive cytotoxic lymphocyte maturation factor."; Proc. Natl. Acad. Sci. U.S.A. 88:4143-4147(1991).
[2]	NUCLEOTIDE SEQUENCE [MRNA]. PubMed=1673147 [NCBI, ExPASy, EBI, Israel, Japan] Wolf S.F., Temple P.A., Kobayashi M., Young D., Dicig M., Lowe L., Dzialo R., Fitz L., Ferenz C., Hewick R.M., Kelleher K., Herrmann S.H., Clark S.C., Azzoni L., Chan S.H., Trinchieri G., Perussia B.; "Cloning of cDNA for natural killer cell stimulatory factor, a heterodimeric cytokine with multiple biologic effects on T and natural killer cells."; J. Immunol. 146:3074-3081(1991).
[3]	NUCLEOTIDE SEQUENCE [GENOMIC DNA]. SeattleSNPs program for genomic applications; Submitted (JUL-2001) to the EMBL/GenBank/DDBJ databases.
[4]	PROTEIN SEQUENCE OF 23-48. PubMed=2204066 [NCBI, ExPASy, EBI, Israel, Japan] Stern A.S., Podlaski F.J., Hulmes J.D., Pan Y.C.E., Quinn P.M., Wolitzky A.G., Familletti P.C., Stremlo D.L., Truitt T., Chizzonite R., Gately M.K.; "Purification to homogeneity and partial characterization of cytotoxic lymphocyte maturation factor from human B-lymphoblastoid cells."; Proc. Natl. Acad. Sci. U.S.A. 87:6808-6812(1990).
[5]	SIMILARITY TO IL-6. DOI=10.1016/0167-5699(92)90140-3; PubMed=1374259 [NCBI, ExPASy, EBI, Israel, Japan] Merberg D.M., Wolf S.F., Clark S.C.; "Sequence similarity between NKSF and the IL-6/G-CSF family."; Immunol. Today 13:77-78(1992).
[6]	X-RAY CRYSTALLOGRAPHY (2.8 ANGSTROMS) OF 23-219, AND DISULFIDE BONDS. DOI=10.1093/emboj/19.14.3530; PubMed=10899108 [NCBI, ExPASy, EBI, Israel, Japan] Yoon C., Johnston S.C., Tang J., Stahl M., Tobin J.F., Somers W.S.; "Charged residues dominate a unique interlocking topography in the heterodimeric cytokine interleukin-12."; EMBO J. 19:3530-3541(2000).

Comments

FUNCTION: Cytokine that can act as a growth factor for activated T and NK cells, enhance the lytic activity of NK/lymphokine-activated Killer cells, and stimulate the production of IFN-gamma by resting PBMC.
SUBUNIT: Heterodimer with IL12B; disulfide-linked. The heterodimer is known as interleukin IL-12.
INTERACTION:
P29460:IL12B; NbExp=1; IntAct=EBI-1029636, EBI-1029614;
SUBCELLULAR LOCATION: Secreted.
SIMILARITY: Belongs to the IL-6 superfamily.
WEB RESOURCE: Name=Wikipedia; Note=Interleukin-12 entry; URL="http://en.wikipedia.org/wiki/Interleukin_12";.
WEB RESOURCE: Name=SeattleSNPs; URL="http://pga.gs.washington.edu/data/il12a/";.

Copyright

Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms. Distributed under the Creative Commons Attribution-NoDerivs License.

Cross-references

Sequence databases

EMBL

M65271; AAA35694.1; -; mRNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
M65291; AAA59937.1; ALT_INIT; mRNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
AF404773; AAK84425.1; -; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]

RefSeq

NP_000873.2; -.

UniGene

Hs.673

3D structure databases

PDB

1F45; X-ray; 2.80 A; B=23-219.

[ExPASy / RCSB / EBI]

PDBsum

1F45; -.

ModBase

P29459.

Protein-protein interaction databases

DIP

DIP:3772N; -.

IntAct

P29459; -.

Organism-specific databases

HIX0030715; -.

HGNC:5969; IL12A.

HPA001886; -.

161560; gene. [NCBI / EBI]

PharmGKB

PA29784; -.

GeneCards

P29459.

Gene expression databases

ArrayExpress

P29459; -.

CleanEx

HS_IL12A; -.

Ontologies

GO:0043514;	Cellular component: interleukin-12 complex (inferred from direct assay from UniProtKB).
GO:0005143;	Molecular function: interleukin-12 receptor binding (non-traceable author statement from UniProtKB).
GO:0045513;	Molecular function: interleukin-27 binding (inferred from physical interaction from UniProtKB).
GO:0046982;	Molecular function: protein heterodimerization activity (inferred from physical interaction from UniProtKB).
GO:0007050;	Biological process: cell cycle arrest (inferred from direct assay from UniProtKB).
GO:0016477;	Biological process: cell migration (inferred from direct assay from UniProtKB).
GO:0050830;	Biological process: defense response to Gram-positive bacterium (inferred from expression pattern from UniProtKB).
GO:0048662;	Biological process: negative regulation of smooth muscle cell proliferation (inferred from direct assay from UniProtKB).
GO:0045785;	Biological process: positive regulation of cell adhesion (inferred from direct assay from UniProtKB).
GO:0032729;	Biological process: positive regulation of interferon-gamma production (inferred from direct assay from UniProtKB).
GO:0050671;	Biological process: positive regulation of lymphocyte proliferation (inferred from direct assay from UniProtKB).
GO:0002860;	Biological process: positive regulation of natural killer cell mediated cytotoxicity directed against tumor cell target (inferred from direct assay from UniProtKB).
GO:0032816;	Biological process: positive regulation of natural killer cell activation (inferred from direct assay from UniProtKB).
GO:0034393;	Biological process: positive regulation of smooth muscle cell apoptosis (inferred from direct assay from UniProtKB).
GO:0001916;	Biological process: positive regulation of T cell mediated cytotoxicity (inferred from direct assay from UniProtKB).
GO:0042520;	Biological process: positive regulation of tyrosine phosphorylation of Stat4 protein (inferred from direct assay from UniProtKB).
GO:0032496;	Biological process: response to lipopolysaccharide (inferred from direct assay from UniProtKB).
GO:0010224;	Biological process: response to UV-B (inferred from direct assay from UniProtKB).
QuickGo view.

Family and domain databases

InterPro

IPR012351; 4_helix_cytokine_core.
IPR004281; IL12.
Graphical view of domain structure.

Gene3D

G3DSA:1.20.1250.10; 4_helix_cytokine_core; 1.

PANTHER

PTHR10523; IL12; 1.

Pfam

PF03039; IL12; 1.
Pfam graphical view of domain structure.

Genome annotation databases

Ensembl

ENSG00000168811; Homo sapiens. [Contig view]

GeneID

3592; -.

KEGG

hsa:3592; -.

Phylogenomic databases

HOVERGEN

P29459; -.

Other

NextBio

14035; -.

SOURCE

IL12A; Homo sapiens.

UniRef

View cluster of proteins with at least 50% / 90% / 100% identity.

Keywords

3D-structure; Cytokine; Direct protein sequencing; Glycoprotein; Growth factor; Secreted; Signal.

Features

Feature table viewer

`Key`	`From To`	`Length`	`Description`	`FTId`
`SIGNAL`	`1 22`	`22`
`CHAIN`	`23 219`	`197`	`Interleukin-12 subunit alpha.`	`PRO_0000015604`
`CARBOHYD`	`93 93`		`N-linked (GlcNAc...) (Potential).`
`CARBOHYD`	`107 107`		`N-linked (GlcNAc...) (Potential).`
`DISULFID`	`64 196`
`DISULFID`	`85 123`
`DISULFID`	`96 96`		`Interchain (with C-199 in IL12B).`
`CONFLICT`	`213 213`		`M -> T (in Ref. 1; AAA35694).`
`HELIX`	`43 58`	`16`
`HELIX`	`59 61`	`3`
`HELIX`	`81 84`	`4`
`HELIX`	`88 92`	`5`
`HELIX`	`118 145`	`28`
`HELIX`	`155 169`	`15`
`HELIX`	`190 217`	`28`

Sequence information

Length: 219 AA [This is the length of the unprocessed precursor]

Molecular weight: 24874 Da [This is the MW of the unprocessed precursor]

CRC64: 7C658AB7716112B2 [This is a checksum on the sequence]

        10         20         30         40         50         60 
MCPARSLLLV ATLVLLDHLS LARNLPVATP DPGMFPCLHH SQNLLRAVSN MLQKARQTLE 

        70         80         90        100        110        120 
FYPCTSEEID HEDITKDKTS TVEACLPLEL TKNESCLNSR ETSFITNGSC LASRKTSFMM 

       130        140        150        160        170        180 
ALCLSSIYED LKMYQVEFKT MNAKLLMDPK RQIFLDQNML AVIDELMQAL NFNSETVPQK 

       190        200        210 
SSLEEPDFYK TKIKLCILLH AFRIRAVTID RVMSYLNAS

P29459 in FASTA format

View entry in original UniProtKB/Swiss-Prot format
View entry in raw text format (no links)
Report form for errors/updates in this UniProtKB/Swiss-Prot entry

	BLAST submission on ExPASy/SIB or at NCBI (USA)		Sequence analysis tools: ProtParam, ProtScale, Compute pI/Mw, PeptideMass, PeptideCutter, Dotlet (Java)
	ScanProsite, MotifScan		Submit a homology modeling request to SWISS-MODEL
	NPSA Sequence analysis tools